Carboxypeptidase A: Difference between revisions

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Further detailed studies of anions have indicated that the nature of anion inhibition in the binding site is partly [http://en.wikipedia.org/wiki/Competitive_inhibition competitive].<ref name="CPA1" />  In particular, the sulfate anion (SO<sub>4</sub><sup>2-</sup>) has been of interest to researchers.  In a crystallized structure of carboxypeptidase T (PDB code: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1ord 1ORD]), a SO<sub>4</sub><sup>2-</sup> anion was found occupying a portion of a region that corresponds to the amino acid residues Arg127, Asn144, Arg145, and Tyr248 of the S1 subsite of carboxypeptidase A.<ref name="CPA1" />  In this case, it is understood that the SO<sub>4</sub><sup>2-</sup> anion prevents the recognition of the carboxylate group at the C-terminus of the polypeptide substrate.
Further detailed studies of anions have indicated that the nature of anion inhibition in the binding site is partly [http://en.wikipedia.org/wiki/Competitive_inhibition competitive].<ref name="CPA1" />  In particular, the sulfate anion (SO<sub>4</sub><sup>2-</sup>) has been of interest to researchers.  In a crystallized structure of carboxypeptidase T (PDB code: [http://www.rcsb.org/pdb/explore/explore.do?structureId=1ord 1ORD]), a SO<sub>4</sub><sup>2-</sup> anion was found occupying a portion of a region that corresponds to the amino acid residues Arg127, Asn144, Arg145, and Tyr248 of the S1 subsite of carboxypeptidase A.<ref name="CPA1" />  In this case, it is understood that the SO<sub>4</sub><sup>2-</sup> anion prevents the recognition of the carboxylate group at the C-terminus of the polypeptide substrate.
==3D structures of carboxypeptidase A==
See [[Carboxypeptidase]]


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Geoffrey C. Hoops, Michael Melbardis, Douglas Schnell, Thomas Baldwin, Michal Harel